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Database: UniProt
Entry: A0A0F8VT51_9EURO
LinkDB: A0A0F8VT51_9EURO
Original site: A0A0F8VT51_9EURO 
ID   A0A0F8VT51_9EURO        Unreviewed;      1604 AA.
AC   A0A0F8VT51;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KKK26411.1};
GN   ORFNames=ARAM_002186 {ECO:0000313|EMBL:KKK26411.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK26411.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK26411.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK26411.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC         complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC         L-lysyl-[glycine-cleavage complex H protein]; Xref=Rhea:RHEA:24304,
CC         Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57305, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83143; EC=1.4.4.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00043839};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR603437-50};
CC   -!- PATHWAY: Purine metabolism; guanine degradation; xanthine from guanine:
CC       step 1/1. {ECO:0000256|ARBA:ARBA00004984}.
CC   -!- SIMILARITY: Belongs to the GcvP family.
CC       {ECO:0000256|ARBA:ARBA00010756}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       ATZ/TRZ family. {ECO:0000256|ARBA:ARBA00006745}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKK26411.1}.
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DR   EMBL; JZBS01000399; KKK26411.1; -; Genomic_DNA.
DR   STRING; 308745.A0A0F8VT51; -.
DR   OrthoDB; 177349at2759; -.
DR   UniPathway; UPA00603; UER00660.
DR   Proteomes; UP000034291; Unassembled WGS sequence.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008892; F:guanine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR   GO; GO:0006147; P:guanine catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00613; GDC-P; 2.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR003437; GcvP.
DR   InterPro; IPR049316; GDC-P_C.
DR   InterPro; IPR049315; GDC-P_N.
DR   InterPro; IPR020581; GDC_P.
DR   InterPro; IPR014311; Guanine_deaminase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00461; gcvP; 1.
DR   NCBIfam; TIGR02967; guan_deamin; 1.
DR   PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034291}.
FT   DOMAIN          79..540
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          560..831
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          882..1003
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
FT   DOMAIN          1153..1553
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   MOD_RES         806
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ   SEQUENCE   1604 AA;  174187 MW;  9DEE556BD7D64646 CRC64;
     MAASWCALRG SRQLALRSRL HPVPSIALRR TTPKTYLPAS RALHTTTTTT RRPVYTSSVA
     DHGVPHPRDI FQPLDTFPRR HIGPSPDAAQ EMLATLDPPV ATLDEFVKQV LPADILSQKD
     LAVTAPSADT GLPRSSVHGG LGETDMLQLL DQYRKQIDVS GKTYIGAGYY PTIVPPVILR
     NILENPAWYT SYTPYQPEIS QGRLESLLNF QTLTADLTGL PFANASVLDE GTAAAEAMTM
     SLATLPAAKQ KRPGKAYVVS HLCHPQTIAV MQSRAEGFGI NLVVGDILAN DHQLVKEQGD
     NLIGVLAQYP DTEGGVYDYQ GLSDTIHATG GTFSVATDLL ALTVLKAPGE FGADIAFGNA
     QRFGVPMGYG GPHAAFFACA DQYKRKVPGR VVGVSKDRLG NRALRLALQT REQHIRREKA
     TSNICTAQAL LANMSAMYAV YHGPAGLKAI AQRIMSMTTT LQTQLAALGF HVPIKSNTQD
     GATLFDTVVV ELSSRDEADA LVAAARAQSI FLRRVSATKV GVSLDETAGR EDVKNILQVF
     ATYATKGEVA LTEPLGLASI PASLARSSAY LTHPVFNTHH SETEMLRYIH HLESKDLSLA
     HSMIPLGSCT MKLNATTEMI PVSWPEFSQM HPFLPADVAQ GYTRMIDDLE QQLADITGMA
     EVTVQPNSGA QGEFAGLRVI KKYLEANGGS KRNICLIPVS AHGTNPASAA MAGMKVVTIK
     CDTKTGNLDL EDLAAKCEKH QEALAAIMIT YPSTFGVYEP GVKQACNLVH QYGGQVYMDG
     ANMNAQIGLC SPGEIGADVC HLNLHKTFCI PHGGGGPGVG PIGVAEHLRP FLPSHPASEY
     LQAKRSESSS PPISAAPWGS ASILPITFNY INMMGAKGLT HATKITLLNA NYILARLKQH
     YPILYTNENG RCAHEFILDV RKFKETCGVE AIDIAKRLQD YGFHAPTMSW PVANTLMIEP
     TESENKAELD RFCDALISIR HEIAAVESGA QPRDGNVLKM APHTQRDLLA TEWDRPYARE
     TAAYPLPYLL EKKFWPSVTR VDDELIESAL DVEDAIVRSE VQMAPTITFF YGTFVHLPRT
     KSGGKHELEI RHGALWVSSA TGRIQGCDWS VSGEEQLQAL IQSQGWVLGA GGGSCEGRVE
     IFRAREEQNE FFFPGFIDTH IHAPQYPNSG LFGSSTLLDW LSTYTFPLES SFGDDSLTKA
     HAIYNQVISR TLANGTTCAS YFATIHVPAT NLLATLCHRR GQRALIGRVC MDNPDFCPDY
     YRDRSAEASL ASTKETITHI HALDPSSKLI HPIITPRFAP TCSRAALASL GALAASHSPP
     LHIQTHISEN KDEVTLVHTL FPESTSYADV YDHHGLLTPR TILAHAVHLT PEEKALIGTR
     HAKVSHCPAS NSALGSGLCP VRSLLDAGIT VGLGTDVSGG YSPSILEAVR QACLVSRLLR
     HSAAPEAEST ANDNRNVLRV EEVLYLATRG GAAVVSMPDD LGGFDPGMFF DAQLIRLGSV
     ESVERQPAGS SCLPNETVVD VFGFESWTEK IHKWVWTGDD RNVRRVWVSG RPVHSLEDGP
     AEEKKGLGSF SATITSRFLF ARPNPNIVLC FHCKRSKTRA VYKE
//
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